|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
11-686 |
0e+00 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 1146.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 11 TETDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGF 90
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 91 GLEMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVAGDGC 170
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRP---GHDIVDHYTYVIAGDGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 171 LQEGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTK 250
Cdd:COG0021 158 LMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 251 PTIVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDvNFPEEDEVIAHTRKLGERAAAARSEWQQRFDAWA 330
Cdd:COG0021 238 PTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 331 EKNPEHKALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFGPE 410
Cdd:COG0021 317 AAYPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 411 SittemftaePYGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGED 490
Cdd:COG0021 397 D---------PSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 491 GPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTKERAfEGVSKGGYVLVDgAK 570
Cdd:COG0021 468 GPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLAD-AE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 571 STPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFTGDHG 650
Cdd:COG0021 546 GTPDVILIATGSEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDG 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 2519076985 651 RNVSLEHFGASAPGAELFERFGFTTEHVVEAARDSL 686
Cdd:COG0021 626 AVIGIDTFGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
7-686 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 916.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 7 PDDWTETDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLY 86
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 87 LGGFGLEMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVA 166
Cdd:PRK05899 81 LAGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRP---GLDIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 167 GDGCLQEGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVEsGEDVAAIEEAVEKAKA 246
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVD-GHDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 247 ETtKPTIVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDtdvnfpeedeviahtrklgERAAaarSEwqqrf 326
Cdd:PRK05899 237 ST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWD-------------------YRKA---SG----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 327 dawaeknpehKALfdrltarelpagwkdefptwepdakgvatrkasaaaiQAAAAALPELWGGSADLAGSNNTLINGAPS 406
Cdd:PRK05899 289 ----------KAL-------------------------------------NALAKALPELVGGSADLAGSNNTKIKGSKD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 407 FGPESITtemftaepyGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIG 486
Cdd:PRK05899 322 FAPEDYS---------GRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 487 LGEDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTKerAFEGVSKGGYVLV 566
Cdd:PRK05899 393 VGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA--QEEGVAKGGYVLR 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 567 DgaksTPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFT 646
Cdd:PRK05899 471 D----DPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYV 546
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2519076985 647 GDHGRNVSLEHFGASAPGAELFERFGFTTEHVVEAARDSL 686
Cdd:PRK05899 547 GLDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
17-683 |
0e+00 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 822.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 17 AVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFGLEMED 96
Cdd:TIGR00232 3 LANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 97 LKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVAGDGCLQEGVT 176
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKP---GFEIVDHYTYVFVGDGCLQEGIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 177 SEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTKPTIVRV 256
Cdd:TIGR00232 160 YEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 257 KTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDvNFPEEDEVIAH-TRKLGERAAAARSEWQQRFDAWAEKNPE 335
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHfKKTVKERGAKAEQEWNELFAAYKKKYPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 336 HKALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFgPESitte 415
Cdd:TIGR00232 319 LAAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HEN---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 416 mftaePYGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGEDGPTHQ 495
Cdd:TIGR00232 394 -----PLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 496 PVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTkerAFEGVSKGGYVLVDGAKstPDV 575
Cdd:TIGR00232 469 PIEQLASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLKDSKG--PDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 576 ILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKaRVSVEAGTAMPWHRFTGDHGRNVSL 655
Cdd:TIGR00232 544 ILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGM 622
|
650 660
....*....|....*....|....*...
gi 2519076985 656 EHFGASAPGAELFERFGFTTEHVVEAAR 683
Cdd:TIGR00232 623 DSFGESAPGDKLFEEFGFTVENVVAKAK 650
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
13-349 |
2.51e-162 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 470.33 E-value: 2.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 13 TDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFGL 92
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 93 EMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAarrERGLFDPDTPAGESPFDHYIYVVAGDGCLQ 172
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIA---ERNLAATYNRPGFDIVDHYTYVFLGDGCLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 173 EGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTKPT 252
Cdd:pfam00456 158 EGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 253 IVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDVNFPEEDEVIAHTRKLGERAAAARSEWQQRFDAWAEK 332
Cdd:pfam00456 238 LIKCRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKA 317
|
330
....*....|....*..
gi 2519076985 333 NPEHKALFDRLTARELP 349
Cdd:pfam00456 318 YPELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
19-287 |
2.14e-119 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 357.20 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 19 DTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFgLEMEDLK 98
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 99 QLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRerglfdpdtpageSPFDHYIYVVAGDGCLQEGVTSE 178
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL-------------LGFDYRVYVLLGDGELQEGSVWE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 179 ACSLAGTQQLGNLILFWDDNGISIEDDTQ-IAFTEDVMARYEAYGWQTLTVEsGEDVAAIEEAVEKAKAETTKPTIVRVK 257
Cdd:cd02012 147 AASFAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD-GHDVEEILAALEEAKKSKGKPTLIIAK 225
|
250 260 270
....*....|....*....|....*....|
gi 2519076985 258 TVIGFPAPNLQNTGAAHGAALGAEEIKLVK 287
Cdd:cd02012 226 TIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
426-545 |
1.31e-35 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 131.07 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 426 LHFGIREHAMGAIMNGIALHGGtRVYGGTFLIFSEYLYPAIRVAALSGIdGYYVFTHDS-IGLGEDGPTHQPVETLTALR 504
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2519076985 505 AIPDLAVIRPADANETSAAWIAALEgREQPKALALSRQNLP 545
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
11-686 |
0e+00 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 1146.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 11 TETDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGF 90
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 91 GLEMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVAGDGC 170
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRP---GHDIVDHYTYVIAGDGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 171 LQEGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTK 250
Cdd:COG0021 158 LMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 251 PTIVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDvNFPEEDEVIAHTRKLGERAAAARSEWQQRFDAWA 330
Cdd:COG0021 238 PTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 331 EKNPEHKALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFGPE 410
Cdd:COG0021 317 AAYPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 411 SittemftaePYGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGED 490
Cdd:COG0021 397 D---------PSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 491 GPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTKERAfEGVSKGGYVLVDgAK 570
Cdd:COG0021 468 GPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLAD-AE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 571 STPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFTGDHG 650
Cdd:COG0021 546 GTPDVILIATGSEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDG 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 2519076985 651 RNVSLEHFGASAPGAELFERFGFTTEHVVEAARDSL 686
Cdd:COG0021 626 AVIGIDTFGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
7-686 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 916.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 7 PDDWTETDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLY 86
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 87 LGGFGLEMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVA 166
Cdd:PRK05899 81 LAGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRP---GLDIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 167 GDGCLQEGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVEsGEDVAAIEEAVEKAKA 246
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVD-GHDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 247 ETtKPTIVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDtdvnfpeedeviahtrklgERAAaarSEwqqrf 326
Cdd:PRK05899 237 ST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWD-------------------YRKA---SG----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 327 dawaeknpehKALfdrltarelpagwkdefptwepdakgvatrkasaaaiQAAAAALPELWGGSADLAGSNNTLINGAPS 406
Cdd:PRK05899 289 ----------KAL-------------------------------------NALAKALPELVGGSADLAGSNNTKIKGSKD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 407 FGPESITtemftaepyGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIG 486
Cdd:PRK05899 322 FAPEDYS---------GRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 487 LGEDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTKerAFEGVSKGGYVLV 566
Cdd:PRK05899 393 VGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA--QEEGVAKGGYVLR 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 567 DgaksTPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFT 646
Cdd:PRK05899 471 D----DPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYV 546
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2519076985 647 GDHGRNVSLEHFGASAPGAELFERFGFTTEHVVEAARDSL 686
Cdd:PRK05899 547 GLDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
17-683 |
0e+00 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 822.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 17 AVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFGLEMED 96
Cdd:TIGR00232 3 LANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 97 LKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVAGDGCLQEGVT 176
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKP---GFEIVDHYTYVFVGDGCLQEGIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 177 SEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTKPTIVRV 256
Cdd:TIGR00232 160 YEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 257 KTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDvNFPEEDEVIAH-TRKLGERAAAARSEWQQRFDAWAEKNPE 335
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHfKKTVKERGAKAEQEWNELFAAYKKKYPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 336 HKALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFgPESitte 415
Cdd:TIGR00232 319 LAAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HEN---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 416 mftaePYGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGEDGPTHQ 495
Cdd:TIGR00232 394 -----PLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 496 PVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTkerAFEGVSKGGYVLVDGAKstPDV 575
Cdd:TIGR00232 469 PIEQLASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLKDSKG--PDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 576 ILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKaRVSVEAGTAMPWHRFTGDHGRNVSL 655
Cdd:TIGR00232 544 ILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGM 622
|
650 660
....*....|....*....|....*...
gi 2519076985 656 EHFGASAPGAELFERFGFTTEHVVEAAR 683
Cdd:TIGR00232 623 DSFGESAPGDKLFEEFGFTVENVVAKAK 650
|
|
| PLN02790 |
PLN02790 |
transketolase |
21-683 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 811.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 21 ARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGF-GLEMEDLKQ 99
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdSVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 100 LRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFD-PDTPAgespFDHYIYVVAGDGCLQEGVTSE 178
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNkPDHKI----VDHYTYCILGDGCQMEGISNE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 179 ACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESG-EDVAAIEEAVEKAKAETTKPTIVRVK 257
Cdd:PLN02790 157 AASLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGnTDYDEIRAAIKEAKAVTDKPTLIKVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 258 TVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDVNFPEEDeVIAHTRKLGERAAAARSEWQQRFDAWAEKNPEHK 337
Cdd:PLN02790 237 TTIGYGSPNKANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPED-VKSHWSKHTKEGAALEAEWNAKFAEYKKKYPEEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 338 ALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFGPESittemf 417
Cdd:PLN02790 316 AELKSLISGELPSGWEKALPTFTPEDPADATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDT------ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 418 taePYGRNLHFGIREHAMGAIMNGIALHG-GTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGEDGPTHQP 496
Cdd:PLN02790 390 ---PEERNVRFGVREHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 497 VETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTkerAFEGVSKGGYVLVD-GAKSTPDV 575
Cdd:PLN02790 467 IEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGT---SIEGVEKGGYVISDnSSGNKPDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 576 ILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFTGDHGRNVSL 655
Cdd:PLN02790 544 ILIGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGV 623
|
650 660
....*....|....*....|....*...
gi 2519076985 656 EHFGASAPGAELFERFGFTTEHVVEAAR 683
Cdd:PLN02790 624 DRFGASAPAGILYKEFGFTVENVVAAAK 651
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
12-683 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 752.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 12 ETDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFG 91
Cdd:PTZ00089 4 AIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 92 LEMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRERGLFDPDtpaGESPFDHYIYVVAGDGCL 171
Cdd:PTZ00089 84 LSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRP---GHPIFDNYVYVICGDGCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 172 QEGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGE-DVAAIEEAVEKAKAETTK 250
Cdd:PTZ00089 161 QEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 251 PTIVRVKTVIGFpAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDVNFPEEDEVIAHTRKLGERAAAARSEWQQRFDAWA 330
Cdd:PTZ00089 241 PKLIIVKTTIGY-GSSKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 331 EKNPEHKALFDRLTARELPAGWKDEFPTWEPDAKGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFGPE 410
Cdd:PTZ00089 320 AAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 411 SittemftaePYGRNLHFGIREHAMGAIMNGIALHGGTRVYGGTFLIFSEYLYPAIRVAALSGIDGYYVFTHDSIGLGED 490
Cdd:PTZ00089 400 S---------PEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGED 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 491 GPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTkerAFEGVSKGGYVLVDgAK 570
Cdd:PTZ00089 471 GPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGS---SIEGVLKGAYIVVD-FT 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 571 STPDVILIASGSEVQYAVEAAKLLaEDNVSARVVSMPSIDWFLEQSEEYQEKILPRAVKARVSVEAGTAMPWHRFTGDHg 650
Cdd:PTZ00089 547 NSPQLILVASGSEVSLCVEAAKAL-SKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH- 624
|
650 660 670
....*....|....*....|....*....|...
gi 2519076985 651 rnVSLEHFGASAPGAELFERFGFTTEHVVEAAR 683
Cdd:PTZ00089 625 --VGISGFGASAPANALYKHFGFTVENVVEKAR 655
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
13-349 |
2.51e-162 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 470.33 E-value: 2.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 13 TDTRAVDTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFGL 92
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 93 EMEDLKQLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAarrERGLFDPDTPAGESPFDHYIYVVAGDGCLQ 172
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIA---ERNLAATYNRPGFDIVDHYTYVFLGDGCLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 173 EGVTSEACSLAGTQQLGNLILFWDDNGISIEDDTQIAFTEDVMARYEAYGWQTLTVESGEDVAAIEEAVEKAKAETTKPT 252
Cdd:pfam00456 158 EGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 253 IVRVKTVIGFPAPNLQNTGAAHGAALGAEEIKLVKEALGFDTDVNFPEEDEVIAHTRKLGERAAAARSEWQQRFDAWAEK 332
Cdd:pfam00456 238 LIKCRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKA 317
|
330
....*....|....*..
gi 2519076985 333 NPEHKALFDRLTARELP 349
Cdd:pfam00456 318 YPELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
19-287 |
2.14e-119 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 357.20 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 19 DTARILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFgLEMEDLK 98
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 99 QLRTWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRerglfdpdtpageSPFDHYIYVVAGDGCLQEGVTSE 178
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL-------------LGFDYRVYVLLGDGELQEGSVWE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 179 ACSLAGTQQLGNLILFWDDNGISIEDDTQ-IAFTEDVMARYEAYGWQTLTVEsGEDVAAIEEAVEKAKAETTKPTIVRVK 257
Cdd:cd02012 147 AASFAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD-GHDVEEILAALEEAKKSKGKPTLIIAK 225
|
250 260 270
....*....|....*....|....*....|
gi 2519076985 258 TVIGFPAPNLQNTGAAHGAALGAEEIKLVK 287
Cdd:cd02012 226 TIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
22-261 |
1.40e-69 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 228.42 E-value: 1.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 22 RILAADAVEHCGSGHPGTAMSLAPLAYTLYQRVMRLDPTDPKWAGRDRFVLSNGHSSLTQYVQLYLGGFgLEMEDLKQLR 101
Cdd:COG3959 16 RRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGY-FPKEELATFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 102 TWGAKTPGHPEYNHTDHVEITTGPLGQGLASAVGMAMAARRerglfdpdtpAGEspfDHYIYVVAGDGCLQEGVTSEACS 181
Cdd:COG3959 95 KLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKL----------DGK---DYRVYVLLGDGELQEGQVWEAAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 182 LAGTQQLGNLILFWDDNGISIEDdtqiaFTEDVM------ARYEAYGWQTLTVEsGEDVAAIEEAVEKAKAETTKPTIVR 255
Cdd:COG3959 162 AAAHYKLDNLIAIVDRNGLQIDG-----PTEDVMsleplaEKWEAFGWHVIEVD-GHDIEALLAALDEAKAVKGKPTVII 235
|
....*.
gi 2519076985 256 VKTVIG 261
Cdd:COG3959 236 AHTVKG 241
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
384-541 |
5.31e-53 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 179.56 E-value: 5.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 384 PELWGGSADLAGSNNTlingapsfgpesittEMFTAEPYGRNLHFGIREHAMGAIMNGIALHGgTRVYGGTFLIFSEYLY 463
Cdd:cd07033 15 PRIVALSADLGGSTGL---------------DKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519076985 464 PAIRV-AALSGIDGYYVFTHDSIGLGEDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREqPKALALSR 541
Cdd:cd07033 79 DQIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
364-546 |
2.91e-50 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 172.73 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 364 KGVATRKASAAAIQAAAAALPELWGGSADLAGSNNTLINGAPSFgpesittemftaEPYGRNLHFGIREHAMGAIMNGIA 443
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHP------------QGAGRVIDTGIAEQAMVGFANGMA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 444 LHGG-TRVYGGTFLIFSEYLYPAIRV-AALSGIDGYYVFTHDSIGLGEDGPTHQPVETLTALRAIPDLAVIRPADANETS 521
Cdd:pfam02779 69 LHGPlLPPVEATFSDFLNRADDAIRHgAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETK 148
|
170 180
....*....|....*....|....*.
gi 2519076985 522 AAWIAALEGREQ-PKALALSRQNLPV 546
Cdd:pfam02779 149 GLLRAAIRRDGRkPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
426-545 |
1.31e-35 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 131.07 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 426 LHFGIREHAMGAIMNGIALHGGtRVYGGTFLIFSEYLYPAIRVAALSGIdGYYVFTHDS-IGLGEDGPTHQPVETLTALR 504
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2519076985 505 AIPDLAVIRPADANETSAAWIAALEgREQPKALALSRQNLP 545
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
384-686 |
3.99e-31 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 123.66 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 384 PELWGGSADLAGSNntlingapsfgpesiTTEMFTAEPYGRNLHFGIREHAMGAIMNGIALhGGTRVYGGTFLIFSEYL- 462
Cdd:COG3958 22 PDIVVLDADLGGST---------------KLDKFAKAFPDRFFNVGIAEQNMVGVAAGLAL-AGKIPFVSTFAPFLTGRa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 463 YPAIRVA-ALSGIDGYYVFTHDSIGLGEDGPTHQPVETLTALRAIPDLAVIRPADANETSAA--WIAALEGreqPKALAL 539
Cdd:COG3958 86 YEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAvrAAAEHDG---PVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 540 SRQNLPVL--EGTKeraFE-GvskGGYVLVDGAkstpDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSI-----DW 611
Cdd:COG3958 163 GRGAVPVVydEDYE---FEiG---KARVLREGK----DVTIIATGIMVAEALEAAELLAKEGISARVINMHTIkpldeEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 612 FLEQSEEYqekilpRAVkarVSVE----AGT-----------AMPwHRFtgdhgRNVSL-EHFGASAPGAELFERFGFTT 675
Cdd:COG3958 233 ILKAARKT------GAV---VTAEehsiIGGlgsavaevlaeNYP-VPL-----RRIGVpDRFGESGSPEELLEKYGLDA 297
|
330
....*....|.
gi 2519076985 676 EHVVEAARDSL 686
Cdd:COG3958 298 EGIVAAAKELL 308
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
562-678 |
5.55e-16 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 74.55 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 562 GYVLVDgaKSTPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSMPSI---DW--FLEQSEEYQEKILPRAVKARVSVEA 636
Cdd:pfam02780 1 GKAEIL--REGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIkplDKetILESVKKTGRLVTVEEAVPRGGFGS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2519076985 637 GTAMPW--HRFTGDHG--RNVSLEHFGASAPGAELFERFGFTTEHV 678
Cdd:pfam02780 79 EVAAALaeEAFDGLDApvLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
486-687 |
2.28e-10 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 63.88 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 486 GL-GEDGPTHQPVETLTALRAIPDLAVIRPADANETSA--AWIAALEGreqPKALALSRQNLPVLEGTKEraFEGVSKG- 561
Cdd:COG1154 420 GLvGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHmlYTALAYDG---PTAIRYPRGNGPGVELPAE--LEPLPIGk 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 562 GYVLVDGAkstpDVILIASGSEVQYAVEAAKLLAEDNVSARVVSM----PsIDwfleqsEEYQEKILpRAVKARVSVEAG 637
Cdd:COG1154 495 GEVLREGK----DVAILAFGTMVAEALEAAERLAAEGISATVVDArfvkP-LD------EELILELA-REHDLVVTVEEG 562
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2519076985 638 TAMpwhrftG-----------DHGRNVSLEHFG--------ASApgAELFERFGFTTEHVVEAARDSLE 687
Cdd:COG1154 563 VLA------GgfgsavleflaDAGLDVPVLRLGlpdrfiehGSR--AELLAELGLDAEGIARAILELLG 623
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
122-258 |
4.19e-10 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 59.19 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 122 TTGPLGQGLASAVGMAMAARrerglfdpdtpagespfDHYIYVVAGDGCLQEgvTSEACSLAGTQQLGNLILFWDDNGIS 201
Cdd:cd00568 44 GFGAMGYGLPAAIGAALAAP-----------------DRPVVCIAGDGGFMM--TGQELATAVRYGLPVIVVVFNNGGYG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519076985 202 IEDDTQIAFTE-----------DVMARYEAYGWQTLTVESGEDVAAieeAVEKAKAEtTKPTIVRVKT 258
Cdd:cd00568 105 TIRMHQEAFYGgrvsgtdlsnpDFAALAEAYGAKGVRVEDPEDLEA---ALAEALAA-GGPALIEVKT 168
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
486-686 |
2.42e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 60.48 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 486 GL-GEDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNlpvLEGTKERAFEGVSKG-GY 563
Cdd:PRK05444 382 GLvGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGN---GVGVELPELEPLPIGkGE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 564 VLVDGAkstpDVILIASGSEVQYAVEAAKLLAednvSARVVSMPSI-----DWFLEQSEEYqEKIlpravkarVSVE--- 635
Cdd:PRK05444 459 VLREGE----DVAILAFGTMLAEALKAAERLA----SATVVDARFVkpldeELLLELAAKH-DLV--------VTVEega 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2519076985 636 ----AGTAMpwHRFTGDHGRNVSLEHFGAS------APGAELFERFGFTTEHVVEAARDSL 686
Cdd:PRK05444 522 imggFGSAV--LEFLADHGLDVPVLNLGLPdefidhGSREELLAELGLDAEGIARRILELL 580
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
35-192 |
1.19e-08 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 57.70 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 35 GHPGTAMSLAPLAYTLYQRVMRLDPTDpkwAGRDRfVLSNGHSSLTQYVQLYLGGfGLEMEDLKQLRTWGAKtPGHPEYN 114
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEG---GGGDL-VYFQGHASPGIYARAFLEG-RLTEEQLDNFRQEVGG-GGLSSYP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 115 HT----DHVEITTGPLGQGLASAVGMAMAAR--RERGLFDPDtpagespfDHYIYVVAGDGCLQEGVTSEACSLAGTQQL 188
Cdd:cd02017 105 HPwlmpDFWEFPTVSMGLGPIQAIYQARFNRylEDRGLKDTS--------DQKVWAFLGDGEMDEPESLGAIGLAAREKL 176
|
....
gi 2519076985 189 GNLI 192
Cdd:cd02017 177 DNLI 180
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
480-606 |
4.28e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 50.11 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 480 FTHDSIGL-GEDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQNLPVLEGTKERAFEGV 558
Cdd:PRK12571 416 FVLDRAGLvGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGTILGI 495
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2519076985 559 SKgGYVLVDGakstPDVILIASGSEVQYAVEAAKLLAEDNVSARVVSM 606
Cdd:PRK12571 496 GK-GRVPREG----PDVAILSVGAHLHECLDAADLLEAEGISVTVADP 538
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
556-608 |
1.04e-05 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 48.99 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2519076985 556 EGVSKGGYVL--VDGAKSTPDVILIASGSEVQYAVEAAKLLAED-NVSARVVSMPS 608
Cdd:PRK09405 709 EGILKGMYKLetAEGKKGKPKVQLLGSGTILREVLEAAEILAEDyGVAADVWSVTS 764
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
480-603 |
2.10e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 47.97 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 480 FTHDSIGL-GEDGPTHQPVETLTALRAIPDLAVIRPADANE--TSAAWIAALEGReqPKALALSRQN---LPVLEGTKER 553
Cdd:PLN02582 453 FAMDRAGLvGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfHMVATAAAIDDR--PSCFRYPRGNgigVQLPPNNKGI 530
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2519076985 554 AFEgVSKgGYVLVDGAkstpDVILIASGSEVQYAVEAAKLLAEDNVSARV 603
Cdd:PLN02582 531 PIE-VGK-GRILLEGE----RVALLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
123-259 |
2.83e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 46.33 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 123 TGPLGQGLASAVGMAMAARRERGlfdpdtpagespfDHYIYVVAGDGCLQEGVTSEACSLAGTQQLgNLILFWDDNGISI 202
Cdd:cd02000 103 NGIVGGQVPLAAGAALALKYRGE-------------DRVAVCFFGDGATNEGDFHEALNFAALWKL-PVIFVCENNGYAI 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519076985 203 EDDTQIAFTEDVMARY-EAYGWQTLTVEsGEDV----AAIEEAVEKAKAEtTKPTIVRVKTV 259
Cdd:cd02000 169 STPTSRQTAGTSIADRaAAYGIPGIRVD-GNDVlavyEAAKEAVERARAG-GGPTLIEAVTY 228
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
556-608 |
3.45e-05 |
|
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 442021 [Multi-domain] Cd Length: 891 Bit Score: 47.38 E-value: 3.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2519076985 556 EGVSKGGYVLVDG-AKSTPDVILIASGSEVQYAVEAAKLLAED-NVSARVVSMPS 608
Cdd:COG2609 710 EGILKGMYLLKEGeGKGKPRVQLLGSGTILREVLAAAELLAEDwGVAADVWSVTS 764
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
122-258 |
3.51e-05 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 46.67 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 122 TTGPLGQGLASAVGMAMAARRERGlfdpdtpagespfDHYIYVVAGDGCLQEGVTSEACSLAGTQQLGNLILFWDDN-GI 200
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRGE-------------DEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGyAI 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2519076985 201 SIEDDTQIAfTEDVMARYEAYGWQTLTVEsGEDV----AAIEEAVEKAKAEtTKPTIVRVKT 258
Cdd:COG1071 192 STPVERQTA-VETIADRAAGYGIPGVRVD-GNDVlavyAAVKEAVERARAG-EGPTLIEAKT 250
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
552-608 |
8.22e-04 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 42.61 E-value: 8.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2519076985 552 ERAFEGVSKGGYVLvDGAKSTPDVILIASGSEVQYAVEAAKLLAED-NVSARVVSMPS 608
Cdd:PRK13012 713 EGAEEGILKGMYRL-AAAAEAPRVQLLGSGAILREVLAAARLLADDwGVDADVWSVTS 769
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
480-596 |
1.27e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 42.01 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 480 FTHDSIGL-GEDGPTHQPVETLTALRAIPDLAVIRPADANE--TSAAWIAALEGReqPKALALSRQN---LPVLEGTKER 553
Cdd:PLN02234 454 FAIDRAGLmGADGPTHCGAFDVTFMACLPNMIVMAPSDEAElfNMVATAAAIDDR--PSCFRYHRGNgigVSLPPGNKGV 531
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2519076985 554 AFEgVSKgGYVLVDGAKstpdVILIASGSEVQYAVEAAKLLAE 596
Cdd:PLN02234 532 PLQ-IGR-GRILRDGER----VALLGYGSAVQRCLEAASMLSE 568
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
109-261 |
3.65e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 40.37 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 109 GHPEYNHTDHVEITTGPLGQGLASAVGMAMAarreRGLfdpdtpAGEspfDHYIYVVAGDGCLQEGVTSEACSLAGTQQl 188
Cdd:PRK12315 98 GYTNPEESEHDFFTVGHTSTSIALATGLAKA----RDL------KGE---KGNIIAVIGDGSLSGGLALEGLNNAAELK- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 189 GNLILFWDDNGISIEDD-----TQIAFTEDVMARYE-----AYGWQTLTVESGEDVAAIEEAVEKAKaETTKPTIVRVKT 258
Cdd:PRK12315 164 SNLIIIVNDNQMSIAENhgglyKNLKELRDTNGQSEnnlfkAMGLDYRYVEDGNDIESLIEAFKEVK-DIDHPIVLHIHT 242
|
...
gi 2519076985 259 VIG 261
Cdd:PRK12315 243 LKG 245
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
419-604 |
5.15e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 39.99 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 419 AEPYGRNLH-FGIREHAMGAIMNGIALHGGTRVYG--GTFLI-----FSEYL----YPAIRVAALSGIDGyyvfthdsig 486
Cdd:PRK12315 315 RKKYPDQYVdVGIAEQESVAFASGIAANGARPVIFvnSTFLQraydqLSHDLainnNPAVMIVFGGSISG---------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519076985 487 lgeDGPTHQPVETLTALRAIPDLAVIRPADANETSAAWIAALEGREQPKALALSRQnlPVLEGTKEraFEGVSKGGYvlv 566
Cdd:PRK12315 385 ---NDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVPEH--GVESGPTV--DTDYSTLKY--- 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 2519076985 567 DGAKSTPDVILIASGSEVQYAVEAAKLLAED-NVSARVV 604
Cdd:PRK12315 455 EVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLI 493
|
|
| |
